SitesBLAST
Comparing GFF2780 FitnessBrowser__Marino:GFF2780 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
1zk1A Structure of r-specific alcohol dehydrogenase (mutant g37d) from lactobacillus brevis in complex with phenylethanol and NAD (see paper)
41% identity, 90% coverage: 22:277/286 of query aligns to 3:250/251 of 1zk1A
- active site: G17 (= G36), S142 (= S164), Y155 (= Y177), K159 (= K181)
- binding 1-phenylethanone: A93 (= A116), N95 (≠ P118), Y155 (= Y177), Y189 (≠ A211)
- binding nicotinamide-adenine-dinucleotide: G13 (= G32), L16 (≠ R35), I18 (= I37), D37 (= D56), H61 (≠ L78), D62 (= D79), S63 (≠ V80), N89 (= N106), A90 (= A107), I92 (= I109), M140 (≠ I162), Y155 (= Y177), G188 (= G210), I190 (= I212), L194 (≠ M216)
1zjzA Structure of r-specific alcohol dehydrogenase (mutant g37d) from lactobacillus brevis in complex with phenylethanol and NAD (see paper)
41% identity, 90% coverage: 22:277/286 of query aligns to 3:250/251 of 1zjzA
- active site: G17 (= G36), S142 (= S164), Y155 (= Y177), K159 (= K181)
- binding nicotinamide-adenine-dinucleotide: G13 (= G32), L16 (≠ R35), I18 (= I37), D37 (= D56), D62 (= D79), N89 (= N106), A90 (= A107), G91 (= G108), I92 (= I109), Y155 (= Y177), G188 (= G210), I190 (= I212), L194 (≠ M216)
- binding (1r)-1-phenylethanol: A93 (= A116), N95 (≠ P118), L152 (≠ A174), Y155 (= Y177)
1zjyA Structure of r-specific alcohol dehydrogenase (mutant g37d) from lactobacillus brevis in complex with phenylethanol and nadh (see paper)
41% identity, 90% coverage: 22:277/286 of query aligns to 3:250/251 of 1zjyA
- active site: G17 (= G36), S142 (= S164), Y155 (= Y177), K159 (= K181)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G13 (= G32), L16 (≠ R35), G17 (= G36), I18 (= I37), D37 (= D56), D62 (= D79), N89 (= N106), A90 (= A107), G91 (= G108), I92 (= I109), Y155 (= Y177), G188 (= G210), I190 (= I212), L194 (≠ M216)
- binding (1r)-1-phenylethanol: A93 (= A116), N95 (≠ P118), L152 (≠ A174), Y155 (= Y177), Y189 (≠ A211)
6y0sAAA R-specific alcohol dehydrogenase (see paper)
41% identity, 90% coverage: 22:277/286 of query aligns to 3:250/251 of 6y0sAAA
1zk4A Structure of r-specific alcohol dehydrogenase (wildtype) from lactobacillus brevis in complex with acetophenone and NADP (see paper)
41% identity, 90% coverage: 22:277/286 of query aligns to 3:250/251 of 1zk4A
- active site: G17 (= G36), S142 (= S164), Y155 (= Y177), K159 (= K181)
- binding 1-phenylethanone: A93 (= A116), Y155 (= Y177), Y189 (≠ A211)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G32), T15 (≠ A34), L16 (≠ R35), I18 (= I37), T36 (≠ S55), G37 (≠ D56), R38 (≠ I57), H61 (≠ L78), D62 (= D79), N89 (= N106), A90 (= A107), G91 (= G108), I92 (= I109), Y155 (= Y177), G188 (= G210), I190 (= I212), T192 (≠ S214), L194 (≠ M216)
7ejiB Crystal structure of kred f147l/l153q/y190p/l199a/m205f/m206f variant and methyl methacrylate complex
38% identity, 90% coverage: 22:277/286 of query aligns to 3:250/251 of 7ejiB
- binding methyl 2-methylprop-2-enoate: S142 (= S164), I143 (≠ R165), Y155 (= Y177), F205 (≠ I231)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G32), T15 (≠ A34), L16 (≠ R35), G17 (= G36), I18 (= I37), R38 (vs. gap), H39 (vs. gap), D62 (= D79), A63 (≠ V80), N89 (= N106), A90 (= A107), V112 (≠ T135), M140 (≠ I162), S142 (= S164), Y155 (= Y177), K159 (= K181), P187 (= P209), P189 (≠ A211), I190 (= I212), T192 (≠ S214), P193 (= P215), L194 (≠ M220)
7ejhA Crystal structure of kred mutant-f147l/l153q/y190p/l199a/m205f/m206f and 2-hydroxyisoindoline-1,3-dione complex
38% identity, 90% coverage: 22:277/286 of query aligns to 5:252/253 of 7ejhA
- binding 2-oxidanylisoindole-1,3-dione: S144 (= S164), I145 (≠ R165), E146 (≠ S166), Y157 (= Y177), V197 (≠ L221), F207 (≠ I231)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G32), T17 (≠ A34), I20 (= I37), R40 (vs. gap), H41 (vs. gap), D64 (= D79), A65 (≠ V80), N91 (= N106), A92 (= A107), V114 (≠ T135), M142 (≠ I162), S144 (= S164), Y157 (= Y177), K161 (= K181), P189 (= P209), G190 (= G210), P191 (≠ A211), I192 (= I212), T194 (≠ S214), P195 (= P215), L196 (≠ M220)
Q6WVP7 NADP-dependent (R)-specific alcohol dehydrogenase; (R)-specific ADH; Ketoreductase; KRED; EC 1.1.1.- from Lentilactobacillus kefiri (Lactobacillus kefiri) (see paper)
38% identity, 90% coverage: 22:277/286 of query aligns to 4:251/252 of Q6WVP7
Sites not aligning to the query:
1nfqA Rv2002 gene product from mycobacterium tuberculosis (see paper)
39% identity, 91% coverage: 22:280/286 of query aligns to 3:242/244 of 1nfqA
- active site: G17 (= G36), S139 (= S164), Y152 (= Y177), K156 (= K181)
- binding Androsterone: L91 (≠ T110), E141 (≠ S166), C149 (≠ A174), Y152 (= Y177), V193 (≠ I231), I197 (≠ E235), F198 (≠ A236)
- binding 1,4-dihydronicotinamide adenine dinucleotide: R16 (= R35), G17 (= G36), M18 (≠ I37), D37 (= D56), L39 (≠ D58), L59 (= L78), D60 (= D79), V61 (= V80), N87 (= N106), A88 (= A107), I137 (= I162), S139 (= S164), Y152 (= Y177), K156 (= K181), P182 (= P209), V185 (≠ I212), T187 (≠ S214), P188 (= P215), M189 (= M216), T190 (vs. gap)
1nffA Crystal structure of rv2002 gene product from mycobacterium tuberculosis (see paper)
39% identity, 91% coverage: 22:280/286 of query aligns to 3:242/244 of 1nffA
- active site: G17 (= G36), S139 (= S164), Y152 (= Y177), K156 (= K181)
- binding nicotinamide-adenine-dinucleotide: G13 (= G32), R16 (= R35), G17 (= G36), M18 (≠ I37), D37 (= D56), I38 (= I57), L39 (≠ D58), L59 (= L78), D60 (= D79), V61 (= V80), N87 (= N106), A88 (= A107), G89 (= G108), I90 (= I109), I137 (= I162), S139 (= S164), Y152 (= Y177), K156 (= K181), P182 (= P209), V185 (≠ I212), T187 (≠ S214), P188 (= P215), M189 (= M216), T190 (vs. gap)
P9WGT1 3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase; NADH-dependent 3alpha, 20beta-hydroxysteroid dehydrogenase; EC 1.1.1.53 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
39% identity, 91% coverage: 22:280/286 of query aligns to 4:243/260 of P9WGT1
- I6 (≠ D24) mutation to T: Maximal improvement in solubility; when associated with M-47 and K-69.
- RGM 17:19 (≠ RGI 35:37) binding
- D38 (= D56) binding
- V47 (≠ L65) mutation to M: Maximal improvement in solubility; when associated with T-6 and K-69.
- DV 61:62 (= DV 79:80) binding
- T69 (≠ I87) mutation to K: Maximal improvement in solubility; when associated with T-6 and M-47.
- N88 (= N106) binding
- S140 (= S164) mutation to A: Complete loss of both oxidation of androsterone and reduction of progesterone; when associated with T6; M-47 and K-69.
- Y153 (= Y177) binding ; mutation to F: Complete loss of both oxidation of androsterone and reduction of progesterone; when associated with T6; M-47 and K-69.
- K157 (= K181) binding
- 183:191 (vs. 209:216, 44% identical) binding
5itvA Crystal structure of bacillus subtilis bacc dihydroanticapsin 7- dehydrogenase in complex with nadh (see paper)
40% identity, 90% coverage: 22:277/286 of query aligns to 4:254/255 of 5itvA
- active site: G18 (= G36), S141 (= S164), Y154 (= Y177), K158 (= K181)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G32), S17 (≠ R35), G18 (= G36), I19 (= I37), D38 (= D56), I39 (= I57), T61 (≠ L78), I63 (≠ V80), N89 (= N106), G91 (= G108), T139 (≠ I162), S141 (= S164), Y154 (= Y177), K158 (= K181), P184 (= P209), G185 (= G210), I186 (≠ A211), I187 (= I212)
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
38% identity, 89% coverage: 23:277/286 of query aligns to 3:247/248 of 6ixmC
- active site: G16 (= G36), S142 (= S164), Y155 (= Y177), K159 (= K181)
- binding nicotinamide-adenine-dinucleotide: G12 (= G32), S15 (≠ R35), G16 (= G36), I17 (= I37), D36 (= D56), I37 (= I57), A61 (≠ L78), D62 (= D79), T63 (≠ V80), N89 (= N106), A90 (= A107), M140 (≠ I162), S142 (= S164), Y155 (= Y177), K159 (= K181), P185 (= P209), A186 (≠ G210), Y187 (≠ A211), I188 (= I212), L192 (≠ M216)
4nbtA Crystal structure of fabg from acholeplasma laidlawii (see paper)
37% identity, 89% coverage: 21:275/286 of query aligns to 1:237/239 of 4nbtA
- active site: G16 (= G36), S132 (= S164), Y145 (= Y177), K149 (= K181)
- binding nicotinamide-adenine-dinucleotide: G12 (= G32), K15 (≠ R35), G16 (= G36), L17 (≠ I37), D36 (= D56), L37 (≠ I57), L52 (= L78), N53 (≠ D79), V54 (= V80), N80 (= N106), A81 (= A107), G82 (= G108), I130 (= I162), S132 (= S164), Y145 (= Y177), K149 (= K181), P177 (= P209), G178 (= G210), I180 (= I212), T182 (≠ S214)
1g6kA Crystal structure of glucose dehydrogenase mutant e96a complexed with NAD+
37% identity, 89% coverage: 21:275/286 of query aligns to 3:250/261 of 1g6kA
- active site: G18 (= G36), S145 (= S164), Y158 (= Y177), K162 (= K181)
- binding nicotinamide-adenine-dinucleotide: T17 (≠ R35), G18 (= G36), L19 (≠ I37), R39 (vs. gap), D65 (= D79), V66 (= V80), N92 (= N106), A93 (= A107), G94 (= G108), M143 (≠ I162), S145 (= S164), Y158 (= Y177), P188 (= P209), G189 (= G210), I191 (= I212), T193 (≠ S214)
3op4A Crystal structure of putative 3-ketoacyl-(acyl-carrier-protein) reductase from vibrio cholerae o1 biovar eltor str. N16961 in complex with NADP+ (see paper)
38% identity, 88% coverage: 23:275/286 of query aligns to 6:244/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G32), S17 (≠ A34), R18 (= R35), I20 (= I37), T40 (≠ I57), N62 (≠ D79), V63 (= V80), N89 (= N106), A90 (= A107), I92 (= I109), V139 (≠ I162), S141 (= S164), Y154 (= Y177), K158 (= K181), P184 (= P209), G185 (= G210), I187 (= I212), T189 (≠ S214), M191 (= M216)
P40288 Glucose 1-dehydrogenase; EC 1.1.1.47 from Priestia megaterium (Bacillus megaterium) (see 2 papers)
36% identity, 89% coverage: 21:275/286 of query aligns to 3:250/261 of P40288
- 11:35 (vs. 29:53, 44% identical) binding
- E96 (≠ T110) mutation E->A,G,K: Heat stable.
- D108 (≠ S128) mutation to N: Heat stable.
- V112 (= V132) mutation to A: Heat stable.
- E133 (≠ K152) mutation to K: Heat stable.
- V183 (≠ C204) mutation to I: Heat stable.
- P194 (= P215) mutation to Q: Heat stable.
- E210 (= E235) mutation to K: Heat stable.
- Y217 (≠ R242) mutation to H: Heat stable.
Sites not aligning to the query:
- 252 Q→L: Heat stable.
- 253 Y→C: Heat stable.
- 258 A→G: Heat stable.
4nbuB Crystal structure of fabg from bacillus sp (see paper)
37% identity, 90% coverage: 20:276/286 of query aligns to 2:243/244 of 4nbuB
- active site: G18 (= G36), N111 (= N136), S139 (= S164), Q149 (≠ A174), Y152 (= Y177), K156 (= K181)
- binding acetoacetyl-coenzyme a: D93 (= D120), K98 (≠ H123), S139 (= S164), N146 (≠ I171), V147 (≠ P172), Q149 (≠ A174), Y152 (= Y177), F184 (≠ A211), M189 (= M216), K200 (≠ E233)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G32), N17 (≠ R35), G18 (= G36), I19 (= I37), D38 (= D56), F39 (≠ I57), V59 (≠ L78), D60 (= D79), V61 (= V80), N87 (= N106), A88 (= A107), G89 (= G108), I90 (= I109), T137 (≠ I162), S139 (= S164), Y152 (= Y177), K156 (= K181), P182 (= P209), F184 (≠ A211), T185 (≠ I212), T187 (≠ S214), M189 (= M216)
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
38% identity, 88% coverage: 23:275/286 of query aligns to 6:240/243 of 4i08A
- active site: G19 (= G36), N113 (= N136), S141 (= S164), Q151 (≠ A174), Y154 (= Y177), K158 (= K181)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G32), S17 (≠ A34), R18 (= R35), I20 (= I37), T40 (≠ I57), N62 (≠ D79), V63 (= V80), N89 (= N106), A90 (= A107), G140 (≠ S163), S141 (= S164), Y154 (= Y177), K158 (= K181), P184 (= P209), G185 (= G210), T189 (≠ S214)
F1SWA0 Zerumbone synthase; EC 1.1.1.326 from Zingiber zerumbet (Shampoo ginger) (Amomum zerumbet) (see paper)
38% identity, 89% coverage: 22:275/286 of query aligns to 2:256/267 of F1SWA0
- S142 (= S164) mutation to A: Strong reduction in oxidoreductase activity toward 8-hydroxy-alpha-humulene and borneol.
- S144 (= S166) mutation to A: Increased oxidoreductase activity toward 8-hydroxy-alpha-humulene and borneol.
- Y155 (= Y177) mutation to A: Strong reduction in oxidoreductase activity toward 8-hydroxy-alpha-humulene and borneol.
- K159 (= K181) mutation to A: Abolishes all oxidoreductase activity.
Query Sequence
>GFF2780 FitnessBrowser__Marino:GFF2780
MYTEIDDLGRRKEIKLGFRMKRLDGKTALITGAARGIGEAIAIQFAEQGATVIVSDIDDQ
MGQALVDSSKLDMHYLHLDVSDESQWITCAKSIEDQFGGLDILVNNAGITGFLESAGPHD
PEHLDLASWETVHATNLNGVALGCKYGIKLMKSSRSASIVNISSRSGLVGIPGAAAYASS
KAGVRNHTKSVALHCAEKGYPIRCNSIHPGAIMSPMWEAMLGEGEAREAAIAEVEAGVPI
GRMGKPEDVAYAALYLASDESNYVTGIELNIDGGILAGSASAPARR
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory